Strong Solute-Solute Dispersive Interactions in a Protein-Ligand Complex

Richard Malham, Sarah Johnstone, Richard J. Bingham, Elizabeth Barratt, Simon E V Phillips, Charles A. Laughton, Steve W. Homans

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67 Citations (Scopus)

Abstract

The contributions of solute-solute dispersion interactions to binding thermodynamics have generally been thought to be small, due to the surmised equality between solute-solvent dispersion interactions prior to the interaction versus solute-solute dispersion interactions following the interaction. The thermodynamics of binding of primary alcohols to the major urinary protein (MUP-I) indicate that this general assumption is not justified. The enthalpy of binding becomes more favorable with increasing chain length, whereas the entropy of binding becomes less favorable, both parameters showing a linear dependence. Despite the hydrophobicity of the interacting species, these data show that binding is not dominated by the classical hydrophobic effect, but can be attributed to favorable ligand-protein dispersion interactions.

Original languageEnglish
Pages (from-to)17061-17067
Number of pages7
JournalJournal of the American Chemical Society
Volume127
Issue number48
DOIs
Publication statusPublished - 7 Dec 2005
Externally publishedYes

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    Malham, R., Johnstone, S., Bingham, R. J., Barratt, E., Phillips, S. E. V., Laughton, C. A., & Homans, S. W. (2005). Strong Solute-Solute Dispersive Interactions in a Protein-Ligand Complex. Journal of the American Chemical Society, 127(48), 17061-17067. https://doi.org/10.1021/ja055454g